1ATU

UNCLEAVED ALPHA-1-ANTITRYPSIN

Summary for 1ATU

• Entry DOI: 10.2210/pdb1atu/pdb
• Descriptor: ALPHA-1-ANTITRYPSIN (1 entity in total)
• Functional Keywords: serine protease inhibitor, alpha-1-antitrypsin, conformational transition, loop flexibility, metastability, stabilizing mutations
• Biological source: Homo sapiens (human)
• Cellular location: Secreted. Short peptide from AAT: Secreted, extracellular space, extracellular matrix: P01009
• Total number of polymer chains: 1
• Total formula weight: 42046.09

Authors

Ryu, S.-E.,Choi, H.-J. (deposition date: 1997-05-11, release date: 1997-08-20, Last modification date: 2024-05-22)

Primary citation

Ryu, S.E.,Choi, H.J.,Kwon, K.S.,Lee, K.N.,Yu, M.H.
The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: crystal structure of an uncleaved alpha1-antitrypsin at 2.7 A.
Structure, 4:1181-1192, 1996

PubMed Abstract: The protein alpha1-antitrypsin is a prototype member of the serpin (serine protease inhibitor) family and is known to inhibit the activity of neutrophil elastase in the lower respiratory tract. Members of this family undergo a large structural rearrangement upon binding to a target protease, involving cleavage of the reactive-site loop. This loop is then inserted into the main body of the enzyme following the opening of a central beta sheet, leading to stabilization of the structure. Random mutageneses of alpha1-antitrypsin identified various mutations that stabilize the native structure and retard the insertion of the reactive-site loop. Structural studies of these mutations may reveal the mechanism of the conformational change.

PubMed: 8939743
DOI: 10.1016/S0969-2126(96)00126-8

Experimental method

X-RAY DIFFRACTION (2.7 Å)